|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
2-365 |
0e+00 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 558.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365 159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365 239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462580778 319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365 315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
3-365 |
2.04e-151 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 458.19 E-value: 2.04e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129 68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129 146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129 223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2462580778 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
9-358 |
4.78e-150 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 453.95 E-value: 4.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225 68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225 146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225 226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
|
330 340 350
....*....|....*....|....*....|..
gi 2462580778 327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225 295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
3-356 |
5.40e-141 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 430.14 E-value: 5.40e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMP 241
Cdd:cd00106 145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
|
330 340 350
....*....|....*....|....*....|....*
gi 2462580778 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106 292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
3-358 |
3.46e-118 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 370.25 E-value: 3.46e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371 148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTW 317
Cdd:cd01371 226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462580778 318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371 294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
3-358 |
4.65e-115 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 362.03 E-value: 4.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372 62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372 140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAntlakkkqvFV 308
Cdd:cd01372 220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2462580778 309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372 291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
3-358 |
4.65e-104 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 332.77 E-value: 4.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370 76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ-A 234
Cdd:cd01370 154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaantlaKKKQVFVPYRDSV 314
Cdd:cd01370 231 KTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462580778 315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370 302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
4-367 |
5.90e-102 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 327.16 E-value: 5.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEGLFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373 144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaantlakkKQVFVPYRDS 313
Cdd:cd01373 221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2462580778 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373 293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
3-358 |
1.63e-101 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 325.06 E-value: 1.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDSEMP 241
Cdd:cd01374 138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374 215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462580778 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374 285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-360 |
8.72e-99 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 317.61 E-value: 8.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366 9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366 71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfds 238
Cdd:cd01366 148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFVPYRDSVLTWL 318
Cdd:cd01366 225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462580778 319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366 288 LQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
1-358 |
9.43e-99 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 317.73 E-value: 9.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYSADTkspdyvsQEMVF 79
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFDPNTT-------QEDVY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369 62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369 140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLT 316
Cdd:cd01369 215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462580778 317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369 284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
1-367 |
9.10e-88 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 288.46 E-value: 9.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEGLFSRINETtrwdEASFRTEVS 149
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364 145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 228 TIKFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakkK 304
Cdd:cd01364 225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580778 305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364 291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
27-508 |
1.21e-79 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 273.15 E-value: 1.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059 18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059 91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059 244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 406 EKLQQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059 394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 2462580778 477 QT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059 474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
|
|
| FHA_KIF16B |
cd22732 |
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ... |
446-562 |
1.03e-78 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438784 [Multi-domain] Cd Length: 117 Bit Score: 254.09 E-value: 1.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462580778 526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
4-392 |
7.59e-74 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 269.50 E-value: 7.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188 100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188 154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188 232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188 309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188 380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454
|
410 420
....*....|....*....|
gi 2462580778 373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188 455 IRQLRDELQRVK---ANGNN 471
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
4-356 |
1.11e-72 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 246.15 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368 78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE 239
Cdd:cd01368 150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaaNTLAKKKQVfVPYRDS 313
Cdd:cd01368 230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2462580778 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368 303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
3-356 |
4.84e-71 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 240.95 E-value: 4.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375 1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEGLFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375 68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375 145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 236 FDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVL 315
Cdd:cd01375 225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462580778 316 TWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375 294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
4-356 |
1.22e-67 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 230.85 E-value: 1.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376 66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:cd01376 142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaantlaKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376 219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
|
330 340 350
....*....|....*....|....*....|....
gi 2462580778 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376 286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
4-356 |
3.99e-67 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 229.49 E-value: 3.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEG----LFSRINETTRWDEasFRTEVS 149
Cdd:cd01367 63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367 141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 230 KFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFV 308
Cdd:cd01367 217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462580778 309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367 280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
|
|
| FHA_KIF16 |
cd22708 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ... |
446-554 |
3.17e-65 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438760 [Multi-domain] Cd Length: 109 Bit Score: 215.60 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 2462580778 526 GVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22708 81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
|
|
| PX_KIF16B_SNX23 |
cd06874 |
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ... |
1127-1230 |
1.57e-59 |
|
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.
Pssm-ID: 132784 Cd Length: 127 Bit Score: 199.91 E-value: 1.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1127 ITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQSATSPLHiNK 1206
Cdd:cd06874 25 ITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQLETYLRNFFSVCLKLPACPLY-PK 103
|
90 100
....*....|....*....|....
gi 2462580778 1207 VGLTLSKHTICEFSPFFKKGVFDY 1230
Cdd:cd06874 104 VGRTLSKATLCDFSPFFRKGVFEN 127
|
|
| FHA_KIF16A_STARD9 |
cd22731 |
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ... |
446-564 |
4.18e-49 |
|
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438783 [Multi-domain] Cd Length: 119 Bit Score: 169.96 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462580778 526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22731 81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
|
|
| FHA_PHLB1 |
cd22713 |
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ... |
438-561 |
1.63e-34 |
|
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438765 Cd Length: 120 Bit Score: 128.21 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTeqdIVLHGLDLESEHCIFENIGGTVTLIPL 517
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462580778 518 sGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713 78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
|
|
| FHA_KIF1 |
cd22705 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ... |
453-553 |
6.16e-32 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438757 [Multi-domain] Cd Length: 101 Bit Score: 120.03 E-value: 6.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEA 532
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 2462580778 533 THLNQGAVILLGRTNMFRFNH 553
Cdd:cd22705 81 TRLKTGSRVILGKNHVFRFNH 101
|
|
| FHA_KIF14 |
cd22707 |
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ... |
450-554 |
7.12e-27 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438759 [Multi-domain] Cd Length: 108 Bit Score: 105.81 E-value: 7.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQI 529
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 2462580778 530 VEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707 84 SEPTVLHHGDRVILGGDHYFRFNHP 108
|
|
| FHA_KIF1A |
cd22726 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ... |
454-562 |
1.06e-25 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438778 [Multi-domain] Cd Length: 115 Bit Score: 103.08 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-----VTLIPLSGSQCSVNGVQ 528
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 2462580778 529 IVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22726 82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
|
|
| FHA_KIF28P |
cd22709 |
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
454-554 |
2.28e-25 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438761 [Multi-domain] Cd Length: 102 Bit Score: 101.52 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLS-GSQCSVNGVQIVEA 532
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 2462580778 533 THLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22709 81 TELHHLDRVILGSNHLYVFVGP 102
|
|
| FHA_KIF1B |
cd22727 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ... |
454-556 |
3.44e-25 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438779 [Multi-domain] Cd Length: 110 Bit Score: 101.27 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIF-----ENIGGTVTLIPLSGSQCSVNGVQ 528
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 2462580778 529 IVEATHLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727 83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
6-288 |
1.18e-23 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 98.96 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363 1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEGLFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363 42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 163 rrkssktfnlrvrehpkegpyvedlskhlVQNYGDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdsempc 242
Cdd:cd01363 100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462580778 243 etvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363 137 -------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| PX_RUN |
cd07277 |
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ... |
1127-1224 |
6.60e-23 |
|
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.
Pssm-ID: 132810 Cd Length: 118 Bit Score: 95.11 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1127 ITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQsaTSPlhinK 1206
Cdd:cd07277 25 IRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKRLQVYLRRVVNTLIQ--TSP----E 98
|
90
....*....|....*...
gi 2462580778 1207 VGLTLSKHTICEFSPFFK 1224
Cdd:cd07277 99 LTACPSKETLIKLLPFFG 116
|
|
| FHA_KIF13 |
cd22706 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ... |
471-554 |
1.53e-20 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438758 [Multi-domain] Cd Length: 101 Bit Score: 87.73 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 471 YHLKEgQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 2462580778 551 FNHP 554
Cdd:cd22706 98 LNCP 101
|
|
| FHA_KIF1C |
cd22728 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ... |
454-553 |
2.09e-18 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438780 [Multi-domain] Cd Length: 102 Bit Score: 81.46 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDAsteqDIVLHGLDLESEHCIFENIGG-----TVTLIPLSGSQCSVNGVQ 528
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNpsgevVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 2462580778 529 IVEATHLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728 78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-1095 |
1.26e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG1196 279 LELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 685 AEKEKfeEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:COG1196 358 AELAE--AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 765 QEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQL 844
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 845 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHD--KESRLLEKHDESVTD-----VTEVPQDFEKIKPVEYRLQYKE 917
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvvEDDEVAAAAIEYLKAakagrATFLPLDKIRARAALAAALARG 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 918 RQLQ-YLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEK 996
Cdd:COG1196 596 AIGAaVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 997 VRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
490
....*....|....*....
gi 2462580778 1077 RINAYIEEEVQRRLQDLHR 1095
Cdd:COG1196 756 LPEPPDLEELERELERLER 774
|
|
| PX_domain |
cd06093 |
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ... |
1113-1192 |
1.08e-15 |
|
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.
Pssm-ID: 132768 [Multi-domain] Cd Length: 106 Bit Score: 73.93 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1113 KLHNGTIQRKLKYEITV---LDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRD 1189
Cdd:cd06093 8 EKVKDGGKKYVVYIIEVttqGGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQLEQYLQS 87
|
...
gi 2462580778 1190 FFS 1192
Cdd:cd06093 88 LLN 90
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
611-1099 |
1.57e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaeke 688
Cdd:COG1196 216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 689 kfeeerlreqqeielqkkRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKE 768
Cdd:COG1196 291 ------------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 769 QVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQLRffEFKRRQLVKL 847
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLERLE--EELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 848 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH 927
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 928 LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQ---------LAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 999 KKEKEI--------------LESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQSGLQASL 1064
Cdd:COG1196 591 ALARGAigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510
....*....|....*....|....*....|....*
gi 2462580778 1065 EAEQEALEKDQERINAYIEEEVQRRLQDLHRVISE 1099
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
|
| FHA_AFDN |
cd22711 |
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
453-554 |
5.45e-15 |
|
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438763 [Multi-domain] Cd Length: 106 Bit Score: 71.97 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--RDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSG-SQCSV 524
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 2462580778 525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
3-162 |
1.27e-14 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 72.25 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796 21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 83 GTdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEGLFSRINETTRwdEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796 77 SQ-LVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
456-564 |
1.06e-12 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438781 [Multi-domain] Cd Length: 109 Bit Score: 65.68 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 456 LIGIDDDLLSTGIILYHLKeGQTYVGRDdasTEQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVGAD---TSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 2462580778 535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729 80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
|
|
| PX_SNX13 |
cd06873 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ... |
1125-1187 |
1.84e-12 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.
Pssm-ID: 132783 Cd Length: 120 Bit Score: 65.37 E-value: 1.84e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1125 YEITVL-------DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYL 1187
Cdd:cd06873 25 YAISVTriypngqEESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYL 94
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
624-937 |
2.21e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 71.69 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 624 RKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLREQQEIEL 703
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 704 QKKRQEEETfLRVQE---ELQRLKELnnnekaekfqifqELDQLQKEKDEQYAKLELEKKR----LEEQEKEQVMLVAHL 776
Cdd:pfam17380 356 EERKRELER-IRQEEiamEISRMREL-------------ERLQMERQQKNERVRQELEAARkvkiLEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 777 EEQLREKQEMIqllRRGEVQWVEEEK-RDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQlvklvnlEKDLV 855
Cdd:pfam17380 422 MEQIRAEQEEA---RQREVRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR-------KRAEE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 856 QQKDILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEK 935
Cdd:pfam17380 492 QRRKILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565
|
..
gi 2462580778 936 QR 937
Cdd:pfam17380 566 SR 567
|
|
| PX |
pfam00787 |
PX domain; PX domains bind to phosphoinositides. |
1131-1188 |
5.94e-12 |
|
PX domain; PX domains bind to phosphoinositides.
Pssm-ID: 459940 Cd Length: 84 Bit Score: 62.64 E-value: 5.94e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 1131 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLR 1188
Cdd:pfam00787 6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQ 63
|
|
| PX |
smart00312 |
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ... |
1109-1188 |
1.23e-11 |
|
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.
Pssm-ID: 214610 Cd Length: 105 Bit Score: 62.36 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1109 KDNEKLHNGTIqrklkYEITVLD--ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG---NKDERVIAERRSHL 1183
Cdd:smart00312 6 KIGDGKHYYYV-----IEIETKTglEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGL 80
|
....*
gi 2462580778 1184 EKYLR 1188
Cdd:smart00312 81 EKYLQ 85
|
|
| PX_IRAS |
cd06875 |
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ... |
1126-1187 |
1.30e-11 |
|
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.
Pssm-ID: 132785 Cd Length: 116 Bit Score: 62.68 E-value: 1.30e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462580778 1126 EITVLDETWTVFRRYSRFREMHKTLKLKYAELAALeFPPKKLFGNKDERVIAERRSHLEKYL 1187
Cdd:cd06875 23 EVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDL-LPPKKLIGNKSPSFVEKRRKELEIYL 83
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
610-870 |
1.55e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 610 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 681
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 682 dLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQyaKLELEKKR 761
Cdd:PTZ00121 1600 -LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKK 1676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 762 LEEQEKEQVMLVAHLEEQLREKQEM--IQLLRRGEvqwvEEEKRDLEGIR----ESLLRVKEARAGGDEDGEELEKAQLR 835
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKE----AEEKKKAEELKkaeeENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462580778 836 FFEFKRRQLVKLVNLEKDLVQQKD---ILKKEVQEEQE 870
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEkeaVIEEELDEEDE 1790
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
610-1092 |
1.93e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 690 FEEERLREQQEIE--LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1196 419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQ---WVEEEKRDLEGIRESLLRVKEARAggDEDGEELEKAQLRFFEFKRRQL 844
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGRATF 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 845 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVP-QDFEKIKPVEYRLQYKERQLQYL 923
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGG 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 924 LQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKE 1003
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1004 ILESREKQQ----------------REALERALARLERRhsaLQRhstLGT-------EIEEQRQKLASLNsgsrEQsgl 1060
Cdd:COG1196 737 LLEELLEEEelleeealeelpeppdLEELERELERLERE---IEA---LGPvnllaieEYEELEERYDFLS----EQ--- 803
|
490 500 510
....*....|....*....|....*....|..
gi 2462580778 1061 QASLEAEQEALEkdqERINAyIEEEVQRRLQD 1092
Cdd:COG1196 804 REDLEEARETLE---EAIEE-IDRETRERFLE 831
|
|
| PX_MONaKA |
cd06871 |
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ... |
1131-1187 |
2.56e-11 |
|
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.
Pssm-ID: 132781 Cd Length: 120 Bit Score: 61.99 E-value: 2.56e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580778 1131 DETWTVFRRYSRFREMHKTLKLKYAELAaleFPPKKLFGNKDERVIAERRSHLEKYL 1187
Cdd:cd06871 35 ENSWQVIRRYNDFDLLNASLQISGISLP---LPPKKLIGNMDREFIAERQQGLQNYL 88
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
364-476 |
3.40e-11 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 63.32 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 2462580778 463 LLSTGIILYHLKEG 476
Cdd:pfam16183 163 PLMSECLLYYIKDG 176
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-905 |
4.13e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 606 RLEFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLA 685
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 686 EKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 766 EKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLV 845
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 846 KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 905
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
456-554 |
4.60e-11 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438782 [Multi-domain] Cd Length: 99 Bit Score: 60.70 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 456 LIGIDDDLLSTGIILYHLKEgQTYVGRDDAsteQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 2462580778 535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
611-919 |
6.97e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.69 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEME-------EKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQE-ESLKRRSFHIE-NKLK 681
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAMERE---RELERIRQEERKRElERIRQEEIAMEiSRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 682 DLlaEKEKFEEERLREQQEIELQKKRQEeetflRVQEELQRLKELNNNEKAEKFQIFQE-LDQLQKEKDEQYAKLELEKK 760
Cdd:pfam17380 379 EL--ERLQMERQQKNERVRQELEAARKV-----KILEEERQRKIQQQKVEMEQIRAEQEeARQREVRRLEEERAREMERV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 761 RLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR-----DLEGIRESLLRVKEARAGGDEDGEELEKAQlr 835
Cdd:pfam17380 452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEERKRKLLEKEMEERQKAI-- 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 836 FFEFKRRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKESRLLEkhDESVTDVTEVPQDFEKIKPVeYRL 913
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEqmRKATEERSRLEAMEREREMMRQIVE--SEKARAEYEATTPITTIKPI-YRP 606
|
....*.
gi 2462580778 914 QYKERQ 919
Cdd:pfam17380 607 RISEYQ 612
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
613-944 |
3.14e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 613 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVEtqRKETEIVQLQIRKQEESlkRRSFHIENKLKDLLAEKEKFEE 692
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL-------KRELSSLQSELR--RIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 693 ERLREQQEI-ELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQ-KEKDEQYAKLELEKKRLEE--QEK 767
Cdd:TIGR02169 738 RLEELEEDLsSLEQEIENVKSELkELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEArlREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 768 EQVMLVAHLEEQLREK--QEMIQLLRRGEVQWVEEEKR--DLEGIRESLL-RVKEARAGGDEDGEELE---------KAQ 833
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKeiQELQEQRIDLKEQIKSIEKEieNLNGKKEELEeELEELEAALRDLESRLGdlkkerdelEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 913
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977
|
330 340 350
....*....|....*....|....*....|....
gi 2462580778 914 --QYKERQLQYL-LQNHLPTLLEEKQrafEILDR 944
Cdd:TIGR02169 978 iqEYEEVLKRLDeLKEKRAKLEEERK---AILER 1008
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
455-551 |
8.75e-10 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 56.51 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 455 HLIGIDDDllsTGIILYHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQ-CSVNGVQIVEAT 533
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGRSPDC---DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNgTFVNGKRITPPV 74
|
90
....*....|....*...
gi 2462580778 534 HLNQGAVILLGRTNmFRF 551
Cdd:cd00060 75 PLQDGDVIRLGDTT-FRF 91
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
611-1113 |
1.85e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKF 690
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 691 EEERLREQQEIELQKKRQEEETFLRVQEELQRLKELnnNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQEKEQv 770
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAE- 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 771 mlvaHLEEQLREKQEMIQLLRRG-EVQWVEEEKRDLEGIR---ESLLRVKEARAGGDE--DGEELEKA-QLRFFEFKRR- 842
Cdd:PTZ00121 1461 ----EAKKKAEEAKKADEAKKKAeEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEakKAEEAKKAdEAKKAEEAKKa 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 843 -QLVKLVNLEK-DLVQQKDILKKeVQEEQEILECLKCEHDKESRL-----LEKHDES-VTDVTEVPQDFEKIKPVEYRLQ 914
Cdd:PTZ00121 1537 dEAKKAEEKKKaDELKKAEELKK-AEEKKKAEEAKKAEEDKNMALrkaeeAKKAEEArIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 915 YKERQLQYLLQNHlptllEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQY-------QANANQLQKLQATFEFT 987
Cdd:PTZ00121 1616 EEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkaeedKKKAEEAKKAEEDEKKA 1690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 988 ANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQrhstLGTEIEEQRQKLASLNSGSREQSGLQASLEAE 1067
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1068 QEALEKDQERINAYIEEEV----QRRLQDLHRVISEGCSTSADTMKDNEK 1113
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELdeedEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
612-872 |
2.00e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 612 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaEK 687
Cdd:TIGR02168 674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--AQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 688 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ---YAKLELEKKRLEE 764
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 765 QEKEQVMLVAHLEEQLREKQEMIQLL---RRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRFFEFK- 840
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELS-EELRELESKr 910
|
250 260 270
....*....|....*....|....*....|....*
gi 2462580778 841 ---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL 872
Cdd:TIGR02168 911 selRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
555-824 |
2.32e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 555 KEAAKLREKRKSGLLSSFSLSMTDLSKSREN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 632
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 633 KQKSDKAELERMQQEVEtqrkETEIVQLQIRKQEESLKRrsfhienKLKDLLAEKEKfeeerlreqqeielqkKRQEEET 712
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKK-------KAEEAKKAEED----------------EKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 713 FLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLRR 792
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEK----KKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKE 1765
|
250 260 270
....*....|....*....|....*....|..
gi 2462580778 793 GEVQWVEEEKRDLEGIRESLLRVKEARAGGDE 824
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PX_SNX20_21_like |
cd07279 |
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ... |
1102-1188 |
5.34e-09 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.
Pssm-ID: 132812 Cd Length: 112 Bit Score: 55.03 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1102 STSADTMKDNEKLHngtiqrkLKYEITV-----LDETWTVF-RRYSRFREMHKTLKLKY-AELAALEFPPKKLFGNKDER 1174
Cdd:cd07279 5 IVSARTVKEGEKKY-------VVYQLAVvqtgdPDTQPAFIeRRYSDFLKLYKALRKQHpQLMAKVSFPRKVLMGNFSSE 77
|
90
....*....|....
gi 2462580778 1175 VIAERRSHLEKYLR 1188
Cdd:cd07279 78 LIAERSRAFEQFLG 91
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-946 |
5.90e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.76 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENK 679
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEEtenlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 680 LKDLLAEKEKFEEErlreQQEIELQKKRQEEETFL-----RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK 754
Cdd:pfam02463 243 QELLRDEQEEIESS----KQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 755 LELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQL 834
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 835 RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQ 914
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340 350
....*....|....*....|....*....|..
gi 2462580778 915 YKERQLQYLLQNHLPTLLEEKQRAFEILDRGP 946
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
606-785 |
6.38e-09 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 59.97 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 606 RLEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetqrKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:pfam15709 347 RLEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ------RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 686 EKEKFEEERLREQQEI-ELQKKRQEEETfLRVQEELQRLKELnNNEKAEKFQIFQELD-------QLQKEKDEQYAKLEL 757
Cdd:pfam15709 417 AQERARQQQEEFRRKLqELQRKKQQEEA-ERAEAEKQRQKEL-EMQLAEEQKRLMEMAeeerleyQRQKQEAEEKARLEA 494
|
170 180
....*....|....*....|....*...
gi 2462580778 758 EKKRleEQEKEQVMLVahLEEQLREKQE 785
Cdd:pfam15709 495 EERR--QKEEEAARLA--LEEAMKQAQE 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
611-1095 |
6.70e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKF 690
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 691 EEERLREQQEIELQKKRQEeetflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEK-DEQYAKLELEKKRLEEQEKEQ 769
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIE-----RLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 770 VMLVAHLEEQLREKQEMIQLLRRGEVQwveeekrdLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRqLVKLVN 849
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQ--------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSELIS 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 850 LEK------DLVQQKDILKKEVQEEQEILECLkcEHDKESRL---------LEKHDESVTDVTEVPQDFEKIKPVEYRLQ 914
Cdd:TIGR02168 531 VDEgyeaaiEAALGGRLQAVVVENLNAAKKAI--AFLKQNELgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 915 YKERQLQYLLQNHLPTLL--EEKQRAFEILDR-----------------------GPLSLDNTLYQVEKEMEEKEEQLAQ 969
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 970 YQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLAS 1049
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462580778 1050 -LNSGSREQSGLQASLEAEQEALEKDQERINAYIEE--EVQRRLQDLHR 1095
Cdd:TIGR02168 769 rLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldELRAELTLLNE 817
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-927 |
7.74e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQ--QEVETQRKETEIVQLQIRKQEESLKRRSFhiENKLKDL 683
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEEL--QEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 684 LAEKEKFEEERLREQQEI-ELQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKR 761
Cdd:TIGR02168 252 EEELEELTAELQELEEKLeELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 762 LEEQEKEQVML----------VAHLEEQLREKQEMIQLLRRGEVQW---VEEEKRDLEGIRESLLRVKEARAGGDEDGEE 828
Cdd:TIGR02168 332 LDELAEELAELeekleelkeeLESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 829 LEKAQLRFFEFKRRQLVKLVNLEKDLVQQkdilkkEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikp 908
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQA------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER--- 482
|
330
....*....|....*....
gi 2462580778 909 VEYRLQYKERQLQYLLQNH 927
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
611-1083 |
1.67e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQKS----------DKAELERMQQEVETQRKETEIVQLQIrKQEESLKRRSFHIENKL 680
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 681 KDLLAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:PRK03918 348 KELEKRLE-------------ELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 761 RLEEQEKEQVMLVAHLEEqLREKQEMIQLLRRgevQWVEEEKRDLegIRESLLRVKEARAGGDEDGEELEKAQLRFfefk 840
Cdd:PRK03918 413 RIGELKKEIKELKKAIEE-LKKAKGKCPVCGR---ELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKEL---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 841 rRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKE--SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 916
Cdd:PRK03918 483 -RELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 917 ERQLQYL---LQNHLPTLLEEKQRAFEILDRGPLSLDnTLYQVEKEMEEKEEQLaqyQANANQLQKLQATFEFT-ANIAR 992
Cdd:PRK03918 562 EKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL---EREEKELKKLEEELDKAfEELAE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQSGLQASLEAEQEALE 1072
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
490
....*....|.
gi 2462580778 1073 KDQERINAYIE 1083
Cdd:PRK03918 718 KALERVEELRE 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
611-820 |
1.68e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG4942 26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 690 FEEE-----RLREQQEIELQKKRQEEETFLR--------VQEELQRLKELNNnEKAEKFQIFQELDQLQKEKDEQYAKLE 756
Cdd:COG4942 106 LAELlralyRLGRQPPLALLLSPEDFLDAVRrlqylkylAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462580778 757 LEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveeEKRDLEGIRESLLRVKEARA 820
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-920 |
1.93e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 606 RLEFERQQREELEKLEskrklieemEEKQKSDKAELERMQQEVETQRKeteivqlQIRKQEESLKRrsfHIEnKLKDLLA 685
Cdd:TIGR02169 202 RLRREREKAERYQALL---------KEKREYEGYELLKEKEALERQKE-------AIERQLASLEE---ELE-KLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 686 EKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLK-ELNNNEK--AEKFQIFQELDQLQKEKDEQYAKLELEKKRL 762
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERsiAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 843 QLVKLVNLE---KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpqdfEKIKPVEYRLQYKERQ 919
Cdd:TIGR02169 418 LSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK------EEYDRVEKELSKLQRE 491
|
.
gi 2462580778 920 L 920
Cdd:TIGR02169 492 L 492
|
|
| PX_SNARE |
cd06897 |
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ... |
1126-1189 |
3.12e-08 |
|
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.
Pssm-ID: 132807 Cd Length: 108 Bit Score: 52.66 E-value: 3.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580778 1126 EITVLDETWTVFRRYSRFREMHKTL-KLKYAELAAlEFPPKKLF--GNKDERVIAERRSHLEKYLRD 1189
Cdd:cd06897 21 QVRLPLRSYTVSRRYSEFVALHKQLeSEVGIEPPY-PLPPKSWFlsTSSNPKLVEERRVGLEAFLRA 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
611-1093 |
3.51e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhIENKLKDLLAEKEKF 690
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 691 EEERLREQQEIELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIF-QELDQLQKEKDEQYAKLELEKKRLEEQEKEq 769
Cdd:COG4717 152 EERLEELRELEEELEELEAELA--ELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQEELEELEEE- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 770 vmlVAHLEEQLrEKQEMIQLLRRGEVQWVeeekrdLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFefkrrQLVKLVN 849
Cdd:COG4717 229 ---LEQLENEL-EAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLL-----ALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 850 LEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKhDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlp 929
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELEEELQ-------- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 930 tLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESRE 1009
Cdd:COG4717 365 -LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1010 --------KQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERINAY 1081
Cdd:COG4717 437 leeeleelEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPP 516
|
490
....*....|..
gi 2462580778 1082 IEEEVQRRLQDL 1093
Cdd:COG4717 517 VLERASEYFSRL 528
|
|
| PX_MDM1p |
cd06876 |
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ... |
1133-1188 |
4.18e-08 |
|
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.
Pssm-ID: 132786 Cd Length: 133 Bit Score: 53.08 E-value: 4.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 1133 TWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDER--VIAERRSHLEKYLR 1188
Cdd:cd06876 56 GWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLKYSKtlLVEERRKALEKYLQ 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
623-907 |
4.89e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 623 KRKLIEEM------EEKQKSDKAELErmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLR 696
Cdd:TIGR02169 155 RRKIIDEIagvaefDRKKEKALEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 697 EQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELE-KKRLEEQEKEQVMLVAH 775
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 776 LEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESLLRVKEARaggDEDGEELEKaqlrffefKRRQLVKLVNLEKDLV 855
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRR---DKLTEEYAE--------LKEELEDLRAELEEVD 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 856 QQKDILKKEVQEEQEILECLKCEHD----KESRLLEKHDESVTDVTEVPQDFEKIK 907
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINelkrELDRLQEELQRLSEELADLNAAIAGIE 433
|
|
| PX_CISK |
cd06870 |
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ... |
1124-1187 |
5.27e-08 |
|
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.
Pssm-ID: 132780 Cd Length: 109 Bit Score: 52.02 E-value: 5.27e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462580778 1124 KYEITVLDETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNK-DERVIAERRSHLEKYL 1187
Cdd:cd06870 24 KVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPAS-NLKIPGKRLFGNNfDPDFIKQRRAGLDEFI 87
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-1099 |
5.76e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 702 ELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLR 781
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 782 EKQEMIqLLRRGEVQWVEEEKRDLE-GIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQK 858
Cdd:PRK03918 242 ELEKEL-ESLEGSKRKLEEKIRELEeRIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 859 DILkKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlPTLLEEKQRA 938
Cdd:PRK03918 321 EEI-NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT-------GLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 939 FEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA---------TFEFTANIARQEEKVRKKEKEILESRE 1009
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1010 KQQREaLERALARLER---RHSALQRHSTLGTEIEEQRQKLASLNSGSREQS--------GLQASLEAEQEALEKDQERI 1078
Cdd:PRK03918 473 EKERK-LRKELRELEKvlkKESELIKLKELAEQLKELEEKLKKYNLEELEKKaeeyeklkEKLIKLKGEIKSLKKELEKL 551
|
410 420 430
....*....|....*....|....*....|
gi 2462580778 1079 NAYIEE---------EVQRRLQDLHRVISE 1099
Cdd:PRK03918 552 EELKKKlaelekkldELEEELAELLKELEE 581
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
706-1081 |
6.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLVAHLEEQLRE 782
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 783 KQEMIQLLRRgEVQWVEEEKRDLEgirESLLRVKEARAG--GDEDGEELEK--AQLRFFEFKRRQLVKLVN-LEKDL--- 854
Cdd:TIGR02169 749 LEQEIENVKS-ELKELEARIEELE---EDLHKLEEALNDleARLSHSRIPEiqAELSKLEEEVSRIEARLReIEQKLnrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 855 VQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVtevpqdfEKIKPVEYRLQYKERQLQYLLQNhlptllee 934
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGD-------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 935 kqrafeiLDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ-KLQATFEFTANIARQEEKVRKKEKEILESRE-KQQ 1012
Cdd:TIGR02169 887 -------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaKLEALEEELSEIEDPKGEDEEIPEEELSLEDvQAE 959
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 1013 REALERALARLERRHSAlqrhstlgtEIEEQRQKLASLNsgsrEQSGLQASLEAEQEALekdQERINAY 1081
Cdd:TIGR02169 960 LQRVEEEIRALEPVNML---------AIQEYEEVLKRLD----ELKEKRAKLEEERKAI---LERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
611-889 |
7.67e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEK-LESKRKLIEEMEEkqksDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:TIGR02168 711 EEELEQLRKeLEELSRQISALRK----DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 690 FEEERLREQQEIELQKKRQEE---------ETFLRVQEELQRLKelnnNEKAEKFQIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDElraeltllnEEAANLRERLESLE----RRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 761 RLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwvEEEKRDlEGIRESLLRVKEARAGGDEDGEELEKAQLRffefk 840
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRS------ELEELS-EELRELESKRSELRRELEELREKLAQLELR----- 930
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462580778 841 rrqlvkLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH 889
Cdd:TIGR02168 931 ------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
608-1189 |
8.85e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETQRKETEIVQLQIRKQEESLKRRSF 674
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 675 HIENKLKDLLAEKEkFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQ---IFQELDQLQKEKDEQ 751
Cdd:TIGR00618 313 HTELQSKMRSRAKL-LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtLTQHIHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 752 YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEmiqlLRRGEVQWVEEEKRdlegireslLRVKEARAGGDEDGEELEK 831
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQQRY---------AELCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 832 AQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHdesVTDVTEVPQDFEKIKPVEY 911
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPA---RQDIDNPGPLTRRMQRGEQ 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 912 RLQYKERQLQYL------LQNHLPTLLEEKQRafEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFE 985
Cdd:TIGR00618 536 TYAQLETSEEDVyhqltsERKQRASLKEQMQE--IQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 986 FTANIaRQEEKVRKKEKEILESREKQQREALEraLARLERRHSAL----QRHSTLGTEIEEQRQKLASLNSGSREQSGLQ 1061
Cdd:TIGR00618 614 QHALL-RKLQPEQDLQDVRLHLQQCSQELALK--LTALHALQLTLtqerVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1062 aSLEAEQEALEKDQERINAyiEEEVQRRLQDLHRVISEGCSTSADTMKDNEKLHNGTIQRKLKYEITVLDETWTVFRRYS 1141
Cdd:TIGR00618 691 -QLTYWKEMLAQCQTLLRE--LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2462580778 1142 RFREMHKTLKLKYAELAALEFPPKKLFgNKDERVIAERRSHLEKYLRD 1189
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEIGQEIPS 814
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
619-833 |
9.57e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 619 KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKrrsfhienKLKDLLAEKEKfeeerlreq 698
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------KLQAEIAEAEA--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 699 qeiELQKKRQEEETFLRVQEE--------------------LQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELE 758
Cdd:COG3883 80 ---EIEERREELGERARALYRsggsvsyldvllgsesfsdfLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462580778 759 KKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSA-EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
612-1099 |
9.80e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 612 QQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVE-----TQRKETEIVQLQIRKQEESLKRRSFHienKLKDLLAE 686
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlQQQKTTLTQKLQSLCKELDILQREQA---TIDTRTSA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 687 KEKFEEERLREQQEIELQKKRQEEETfLRVQEELQRLKeLNNNEKAEKFQIFQELDQLQKEKdEQYAKLELEKKRLEEQE 766
Cdd:TIGR00618 419 FRDLQGQLAHAKKQQELQQRYAELCA-AAITCTAQCEK-LEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLAR 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 767 K-EQVMLVAHLEEQLRE-KQEMIQLLRRG-----------EVQWVEEEKRDLEGIRESLL-RVKEARAGGDEDGEELEKA 832
Cdd:TIGR00618 496 LlELQEEPCPLCGSCIHpNPARQDIDNPGpltrrmqrgeqTYAQLETSEEDVYHQLTSERkQRASLKEQMQEIQQSFSIL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 833 QLRFFEFK-------------RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEV 899
Cdd:TIGR00618 576 TQCDNRSKedipnlqnitvrlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 900 PQDFEKIKpveyRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAnqLQK 979
Cdd:TIGR00618 656 TQERVREH----ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA--SSS 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 980 LQATFEFTANIARQeekvrkkekeILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQSG 1059
Cdd:TIGR00618 730 LGSDLAAREDALNQ----------SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2462580778 1060 LQASLEAEQEALEKDQERINAYIEEEVQRRLQDLHRVISE 1099
Cdd:TIGR00618 800 LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE 839
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
706-1077 |
1.27e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 706 KRQEEETFLR---VQEELQRL----KELNNN--------EKAEKFQ-IFQELDQLQ--------KEKDEQYAKLELEKKR 761
Cdd:TIGR02168 171 KERRKETERKlerTRENLDRLedilNELERQlkslerqaEKAERYKeLKAELRELElallvlrlEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 762 LEEQEKEqvmlvahLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEaraggdedgeELEKaQLRFFEFKR 841
Cdd:TIGR02168 251 AEEELEE-------LTAELQELEEKLEELRL-EVSELEEEIEELQKELYALANEIS----------RLEQ-QKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 842 RQLV-KLVNLEKDLV---QQKDILKKEVQEEQEILECLKCEHDkesRLLEKHDESVtdvtevpqdfEKIKPVEYRLQYKE 917
Cdd:TIGR02168 312 ANLErQLEELEAQLEeleSKLDELAEELAELEEKLEELKEELE---SLEAELEELE----------AELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 918 RQLQYLlqnhlptlleeKQRAFEILdrgplsldntlyqvekemeekeeqlAQYQANANQLQKLQATFEftaNIARQEEKV 997
Cdd:TIGR02168 379 EQLETL-----------RSKVAQLE-------------------------LQIASLNNEIERLEARLE---RLEDRRERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 998 RKKEKEILESREKQQREALERALARLER-RHSALQRHSTLGTEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
.
gi 2462580778 1077 R 1077
Cdd:TIGR02168 500 N 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-1192 |
3.09e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 606 RLEFERQQREELEKLESKRKLIE----------EMEEKQKSDKAELERMQQEV---ETQRKETEIVQLQIRKQEESLKRR 672
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEirkfeearmaHFARRQAAIKAEEARKADELkkaEEKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 673 SfhiENKLKdllaeKEKFEEERLREQQEIELQKKRQEEEtflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEkdEQY 752
Cdd:PTZ00121 1311 A---EEAKK-----ADEAKKKAEEAKKKADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE--EAK 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 753 AKLELEKKRLEEQEKeqvmlvahlEEQLREKQEMIQlLRRGEVQWVEEEKRDLEGIRESLLRVKEARAgGDEDGEELEKA 832
Cdd:PTZ00121 1378 KKADAAKKKAEEKKK---------ADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 833 QlrffEFKRR--QLVKLVNLEKDLVQQK--DILKKEVQEEQEILECLKC--EHDKESRLLEKHDESVTDVTEVPQDFEKI 906
Cdd:PTZ00121 1447 D----EAKKKaeEAKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 907 KPVEYRLQYKERQLQYLLQnhlptlLEEKQRAFEIldrgplsldNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEF 986
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKK------AEEKKKADEL---------KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 987 TANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQSGLQASLEA 1066
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1067 EQEALEKDQERINAYIEEEVQRRLQDLHRVISEGCST------SADTMKDNEKLHNGTIQRKLKYEITVLDETWTvfRRY 1140
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeelkkkEAEEKKKAEELKKAEEENKIKAEEAKKEAEED--KKK 1745
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1141 SRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAE--------RRSHLEKYLRDFFS 1192
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedekRRMEVDKKIKDIFD 1805
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
471-551 |
3.24e-07 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 49.57 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716 16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90
|
...
gi 2462580778 549 FRF 551
Cdd:COG1716 91 LRF 93
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
610-870 |
3.74e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI--RKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:pfam13868 30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 688 EKFEEERLREQQEIELQKKRQEEETFLRVQE---ELQRLKELNNNEKAEKFqifqeldqlQKEKDEQYAKLELEKKRL-E 763
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAewkELEKEEEREEDERILEY---------LKEKAEREEEREAEREEIeE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 764 EQEKEQVMLVAHLEEQLREKQEMIQLLRRG-----EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR--- 835
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEree 260
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462580778 836 -FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQE 870
Cdd:pfam13868 261 eEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| PX_SNX15_like |
cd06881 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ... |
1135-1187 |
5.59e-07 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.
Pssm-ID: 132791 Cd Length: 117 Bit Score: 49.63 E-value: 5.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580778 1135 TVFRRYSRFREMHKTLKLKYAELAALE----FPPKKLFGNKDERVIAERRSHLEKYL 1187
Cdd:cd06881 39 VVWKRYSDFKKLHRELSRLHKQLYLSGsfppFPKGKYFGRFDAAVIEERRQAILELL 95
|
|
| PX_SNX19_like_plant |
cd06872 |
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ... |
1125-1189 |
5.64e-07 |
|
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.
Pssm-ID: 132782 Cd Length: 107 Bit Score: 49.06 E-value: 5.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 1125 YEITVLD---ETWTVFRRYSRFREMHKtlKLKYAELAALEFPPKKLFGNK-DERVIAERRSHLEKYLRD 1189
Cdd:cd06872 21 YSVAVTDnenETWVVKRRFRNFETLHR--RLKEVPKYNLELPPKRFLSSSlDGAFIEERCKLLDKYLKD 87
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
451-554 |
6.37e-07 |
|
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438764 [Multi-domain] Cd Length: 120 Bit Score: 49.61 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGRDDASTEQ-DIVLHGLDLESEHCI-----------FENIGGT-- 511
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462580778 512 --VTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712 76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-818 |
6.42e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVqlqiRKQEESLKRRSFHIENKLKDLLA 685
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLER 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 686 EKEkfeeERLREQQEIELQKKRQEEEtflrvqeeLQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168 832 RIA----ATERRLEDLEEQIEELSED--------IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462580778 766 EKEqvmlVAHLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:TIGR02168 900 SEE----LRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQER 944
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
612-1106 |
7.64e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 612 QQREELEKLESKRKL----IEEMEEKQKSDKAELE----RMQQEVETQRKETEIVQLQIR-----------KQEESLKRR 672
Cdd:pfam05483 265 ESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEdikmSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 673 SFH--IENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE 750
Cdd:pfam05483 345 AAHsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 751 QyAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGD----EDG 826
Cdd:pfam05483 424 K-KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 827 EELEKAQLRFFEFKRRQlVKLVNLEKdlvqQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTdvTEVPQDFEKI 906
Cdd:pfam05483 503 ELTQEASDMTLELKKHQ-EDIINCKK----QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK--CKLDKSEENA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 907 KPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRAFEILDRGPLSLdntlyqvEKEMEEKEEQLAQYQANANQLQ-----K 979
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLElelasA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 980 LQATFEFTANIARQEEKVRKKEKEILESREKQ----------QREALERALARLERRHSALQRHSTLGTEIEEQR-QKLA 1048
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERdSELG 728
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 1049 SLNSGSREQSGLQASLEAEQEALEKDQERINAYIEEEVQRRlQDLHRVISEGCSTSAD 1106
Cdd:pfam05483 729 LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK-EKLKMEAKENTAILKD 785
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
609-891 |
7.89e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 609 FERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEV---ETQRKETEIVQLQIRKQEESLKRrsfhIENKLKdllA 685
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaEEARKAEDAKRVEIARKAEDARK----AEEARK---A 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 686 EKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKRLE 763
Cdd:PTZ00121 1173 EDAK------------KAEAARKAEE--VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 764 EQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 843
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462580778 844 LVKlvNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 891
Cdd:PTZ00121 1319 EAK--KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
608-819 |
8.12e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI---RKQEESLKRRSFH-----IENK 679
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhklEEALNDLEARLSHsripeIQAE 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 680 LKDLlaEKEKFEEERLREQQEIELQKKRQEEETflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:TIGR02169 800 LSKL--EEEVSRIEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580778 760 KRLEEQEKEQVML---VAHLEEQLREKQEmiqllRRGEVQWVEEEKRDLEGIRESLLRVKEAR 819
Cdd:TIGR02169 875 AALRDLESRLGDLkkeRDELEAQLRELER-----KIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
615-1090 |
9.82e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 615 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEER 694
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 695 LREQQEIELQK-------KRQEEETFLRVQEELQrlKELNNNEKAEKFQIFQE-LDQLQKEKDEQYAKLElEKKRLEEQE 766
Cdd:TIGR00618 250 EAQEEQLKKQQllkqlraRIEELRAQEAVLEETQ--ERINRARKAAPLAAHIKaVTQIEQQAQRIHTELQ-SKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 767 KEQVMLVAHLEEQLREKQEMIQLLRRGEV---QWVEEEK----------------RDLEGIRESLLRvKEARAGGDEDGE 827
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIhirDAHEVATsireiscqqhtltqhiHTLQQQKTTLTQ-KLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 828 ELEKAQLRFFEFKRRQL-VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE---SVTDVTEVPQDF 903
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEreqQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 904 EKIKPVEYRLQYKERQLQYLLQNhlpTLLEEKQRAFEILDRGPLS--LDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQ 981
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCG---SCIHPNPARQDIDNPGPLTrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 982 ATFEF---TANIARQEEKVRKKEKEILESREKQQREALErALARLERRHSALQRHSTLGTEIEEQRQKLA-SLNSGSREQ 1057
Cdd:TIGR00618 563 EQMQEiqqSFSILTQCDNRSKEDIPNLQNITVRLQDLTE-KLSEAEDMLACEQHALLRKLQPEQDLQDVRlHLQQCSQEL 641
|
490 500 510
....*....|....*....|....*....|...
gi 2462580778 1058 SGLQASLEAEQEALEKDQERINAYIEEEVQRRL 1090
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-891 |
1.01e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQeeSLKRRSFHIENKLKDLL 684
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQEEEL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 685 AEKEKFEEERLREQQEIELQKKRQEEEtflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ--YAKLELEKKRL 762
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKI-----KEEELEELALELKEEQKLEKLAEEELERLEEEITKeeLLQELLLKEEE 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQ---------WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeekeneieeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEE 958
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 891
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
611-787 |
1.36e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEKF 690
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 691 EEERLREQQE---------IELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:COG1579 79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180
....*....|....*....|....*...
gi 2462580778 760 KRLEEQEKEqvmLVAHLEEQLREKQEMI 787
Cdd:COG1579 159 EELEAEREE---LAAKIPPELLALYERI 183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
605-1084 |
1.92e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLESKrklIEEMEEKQKSDKAELERMQQEVETQRKETEivqlqirkqeeslkrrsfHIENKLKDLL 684
Cdd:PRK02224 241 EVLEEHEERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLE------------------ELEEERDDLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 685 AEKEKFEEERLREQQEIELQKKRqEEETFLRVQEELQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAELESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 765 QEKEQVMLVAHLEEQLREKqemiqllrRGEVQWVEEEKRDLEGIRESLLrvkEARAGGDEDGEELEkaqlrffefkrrql 844
Cdd:PRK02224 378 AVEDRREEIEELEEEIEEL--------RERFGDAPVDLGNAEDFLEELR---EERDELREREAELE-------------- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 845 VKLVNLEKDlvqqkdilkkeVQEEQEILE---CLKCEHD-KESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQL 920
Cdd:PRK02224 433 ATLRTARER-----------VEEAEALLEagkCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 921 QYL--LQNHLPTLLEEKQRAFEILDRGPLSLDNTlyqvekemeekEEQLAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:PRK02224 502 EDLveAEDRIERLEERREDLEELIAERRETIEEK-----------RERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 999 KKEKEILESRekqqREALERALARLERRHSALQRHSTLGTEIE---EQRQKLASLNSGSREQ--------SGLQASLEAE 1067
Cdd:PRK02224 571 REEVAELNSK----LAELKERIESLERIRTLLAAIADAEDEIErlrEKREALAELNDERRERlaekrerkRELEAEFDEA 646
|
490
....*....|....*...
gi 2462580778 1068 Q-EALEKDQERINAYIEE 1084
Cdd:PRK02224 647 RiEEAREDKERAEEYLEQ 664
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
611-1132 |
4.37e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQ---QEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 686
Cdd:TIGR02169 335 LAEIEELEReIEEERKRRDKLTEEYAELKEELEDLRaelEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 687 KEKFEEERLREQQEIE--LQKKRQEEETFLRVQEE-------LQRLKELNNNEKAEKFQIFQELDQLQKE---KDEQYAK 754
Cdd:TIGR02169 415 LQRLSEELADLNAAIAgiEAKINELEEEKEDKALEikkqewkLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 755 LELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEK---------RDLEGIR 809
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAvakeaiellKRRKAGR 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 810 ESLLRVKEARAGGDEDGEELEKAQLRF---------------------------FEFKRRQL--VKLVNLEKDLVQQ--- 857
Cdd:TIGR02169 575 ATFLPLNKMRDERRDLSILSEDGVIGFavdlvefdpkyepafkyvfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsga 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 858 --------------KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESvtdVTEVPQDFEKIKPVEYRLQYKERQLQYL 923
Cdd:TIGR02169 655 mtggsraprggilfSRSEPAELQRLRERLEGLKRE---LSSLQSELRRI---ENRLDELSQELSDASRKIGEIEKEIEQL 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 924 LQNH--LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQATFEFTANIAR 992
Cdd:TIGR02169 729 EQEEekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVS 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 993 QEEKVRKKEKEILESREkQQREALERALARLERRHSALQ-RHSTLGTEIEEQRQKLASLNSGSREQSGLQASLEAEQEAL 1071
Cdd:TIGR02169 809 RIEARLREIEQKLNRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462580778 1072 EKDQERINAYIeEEVQRRLQDLhrvisegcSTSADTMKDNEKLHNGTIQrKLKYEITVLDE 1132
Cdd:TIGR02169 888 KKERDELEAQL-RELERKIEEL--------EAQIEKKRKRLSELKAKLE-ALEEELSEIED 938
|
|
| PX_SNX25 |
cd06878 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ... |
1134-1187 |
5.35e-06 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.
Pssm-ID: 132788 Cd Length: 127 Bit Score: 46.98 E-value: 5.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 1134 WTVFRRYSRFREMHKTLKLKYAELAALEFP--PKKLFGNKDERVIAERRSHLEKYL 1187
Cdd:cd06878 50 WVVTRKLSEFHDLHRKLKECSSWLKKVELPslSKKWFKSIDKKFLDKSKNQLQKYL 105
|
|
| PX_SNX20 |
cd07300 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ... |
1118-1193 |
5.63e-06 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.
Pssm-ID: 132833 Cd Length: 114 Bit Score: 46.73 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1118 TIQRKLKYEITVL------DETWTVFRRYSRFREMHKTLKLKYAE-LAALEFPPKKLFGNKDERVIAERRSHLEKYLRDF 1190
Cdd:cd07300 14 TISKHVVYQIIVIqtgsfdCNKVVIERRYSDFLKLHQELLSDFSEeLEDVVFPKKKLTGNFSEEIIAERRVALRDYLTLL 93
|
...
gi 2462580778 1191 FSV 1193
Cdd:cd07300 94 YSL 96
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
610-803 |
6.20e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRR-----SFHIENKLKDLL 684
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyRLGRQPPLALLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 685 AEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQE-------LDQLQKEKDEQYAKLEL 757
Cdd:COG4942 127 SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEleeeraaLEALKAERQKLLARLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462580778 758 EKKRLEEQekeqvmlvahLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG4942 207 ELAELAAE----------LAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
610-1126 |
6.77e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 610 ERQQREELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDllAEK 687
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKD--AEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 688 EKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:PTZ00121 1242 AK------------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 768 --EQVMLVAHLEEQLREKQEMIQLLRRG--EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 843
Cdd:PTZ00121 1310 kaEEAKKADEAKKKAEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 844 LVKLVNLEKDLVQQK---DILKKEVQEEQEILEC-LKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQ 919
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 920 LQyllQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEK 996
Cdd:PTZ00121 1470 KK---ADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 997 VRKKEKEILESREKQQREALERALARLERRHSALQRHSTLgTEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1077 RinayIEEEVQRRLQDLHRVISEGCSTSADTMKDNEKLHNGTIQRKLKYE 1126
Cdd:PTZ00121 1626 K----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| PX_SNX8_Mvp1p_like |
cd06866 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ... |
1106-1189 |
6.86e-06 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.
Pssm-ID: 132776 Cd Length: 105 Bit Score: 46.07 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1106 DTMKDNEKLH-NGTIQRKLKYEITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLE 1184
Cdd:cd06866 1 DTVTVELVPEkKGLFLKHVEYEVSSKRFKSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLS 80
|
....*
gi 2462580778 1185 KYLRD 1189
Cdd:cd06866 81 RFLNL 85
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
605-1099 |
7.38e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLeskrklIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIR----KQEESLKRRSFHIENKL 680
Cdd:COG4913 281 LRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 681 KDLLAEKEKFEEERLREQQEIELqkkrqEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPA-----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 761 RLEEQ----EKEQVMLVAHLEEQLREKQ-------EMIQLlRRGEVQW----------------VEEEKRD--------- 804
Cdd:COG4913 430 SLERRksniPARLLALRDALAEALGLDEaelpfvgELIEV-RPEEERWrgaiervlggfaltllVPPEHYAaalrwvnrl 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 805 -------LEGIRESLLRVKEARAGGD------------------------------EDGEELE------------KAQLR 835
Cdd:COG4913 509 hlrgrlvYERVRTGLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvDSPEELRrhpraitragqvKGNGT 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 836 FFE-----FKRRQLV-------KLVNLEKDLVQqkdiLKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDF 903
Cdd:COG4913 589 RHEkddrrRIRSRYVlgfdnraKLAALEAELAE----LEEELAEAEERLE----ALEAELDALQERREALQRLAEYSWDE 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 904 EKIKPVEYRLQYKERQLQYLLQNH--LPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQ 981
Cdd:COG4913 661 IDVASAEREIAELEAELERLDASSddLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 982 ATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRhstlgtEIEEQRQKLASLNSGsrEQSGLQ 1061
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE------ELERAMRAFNREWPA--ETADLD 808
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2462580778 1062 ASLEA-----------EQEALEKDQERINAYIEEEVQRRLQDLHRVISE 1099
Cdd:COG4913 809 ADLESlpeylalldrlEEDGLPEYEERFKELLNENSIEFVADLLSKLRR 857
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
627-782 |
8.59e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 627 IEEMEEKQKSDkaELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKfeeerLREQQEIELQKK 706
Cdd:COG2433 382 LEELIEKELPE--EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-ELEAELEEKDE-----RIERLERELSEA 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 707 RQEEETFLRVQEELQRLKELNNNEKAEkfqifqeLDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE 782
Cdd:COG2433 454 RSEERREIRKDREISRLDREIERLERE-------LEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKE 522
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
471-555 |
1.01e-05 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 45.33 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87
|
....*..
gi 2462580778 549 FRFNHPK 555
Cdd:pfam16697 88 FCLVPAD 94
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
799-1099 |
1.25e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 799 EEEKRDLEGIRESLLRVKEARaggdedgEELEKaQLRFFEFKRRQLVKLVNLEKDLVQ-QKDILKKEVQEEQEILECLKc 877
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDIL-------NELER-QLKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQ- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 878 ehDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH------LPTLLEEKQRAFEILDRGPLSLDN 951
Cdd:TIGR02168 246 --EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneisrLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 952 TLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaniarQEEKVRKKEKEILESREKQQREALERA------------ 1019
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLrskvaqlelqia 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1020 -----LARLERRHSALQ-RHSTLGTEIEEQRQKL---------ASLNSGSREQSGLQASLEAEQEALEKDQERINAyIEE 1084
Cdd:TIGR02168 397 slnneIERLEARLERLEdRRERLQQEIEELLKKLeeaelkelqAELEELEEELEELQEELERLEEALEELREELEE-AEQ 475
|
330
....*....|....*
gi 2462580778 1085 EVQRRLQDLHRVISE 1099
Cdd:TIGR02168 476 ALDAAERELAQLQAR 490
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
608-806 |
1.60e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETQRKETEivqLQIRKQEESLKRrsfhiENKLkdllaeK 687
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLER-----AEKM------R 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 688 EKFEEERLREQQEIELQKKRQEEETFLRVQEEL-QRLKELNNNEKAEKFQ--IFQELDQLQKEKDEQYA-KLELEKKRLE 763
Cdd:pfam15709 376 EELELEQQRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQeeFRRKLQELQRKKQQEEAeRAEAEKQRQK 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462580778 764 EQE----KEQVMLVAHLEEQ----LREKQEMIQllrrgEVQWVEEEKRDLE 806
Cdd:pfam15709 456 ELEmqlaEEQKRLMEMAEEErleyQRQKQEAEE-----KARLEAEERRQKE 501
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
576-906 |
2.25e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 576 MTDLSKSRENLSAVMLynpglfPIKGPICLRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKET 655
Cdd:pfam05483 337 MEELNKAKAAHSFVVT------EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 656 EIV------QLQIRKQEESLKRRSFHIENKLKDLLAEKEKfeeerLREQQEIELQKKRQEEETFLRVQEELQRLKElnnN 729
Cdd:pfam05483 411 KKIlaedekLLDEKKQFEKIAEELKGKEQELIFLLQAREK-----EIHDLEIQLTAIKTSEEHYLKEVEDLKTELE---K 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 730 EKAEKFQIFQELDqlqkekdeqyaKLELEKKRLEEQEKEQVM-LVAHLEEQLREKQEMIQLLRRGE-VQWVEEEKRD-LE 806
Cdd:pfam05483 483 EKLKNIELTAHCD-----------KLLLENKELTQEASDMTLeLKKHQEDIINCKKQEERMLKQIEnLEEKEMNLRDeLE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 807 GIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLL 886
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
330 340
....*....|....*....|....
gi 2462580778 887 EKHDESVT----DVTEVPQDFEKI 906
Cdd:pfam05483 632 NAYEIKVNklelELASAKQKFEEI 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
607-1099 |
2.58e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAE 686
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELE-ELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 687 KEKFEEERLREQQEIELQKKRQEEetflRVQEELQRLKELNNNEKaekfqifqELDQLqKEKDEQYAKLELE----KKRL 762
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEE----RIEELKKEIEELEEKVK--------ELKEL-KEKAEEYIKLSEFyeeyLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 763 EEQEKEqvmlVAHLEEQLREKQEMIQLL--RRGEVQWVEEE----KRDLEGIRESLLRVKEARAGGDE--------DGEE 828
Cdd:PRK03918 310 REIEKR----LSRLEEEINGIEERIKELeeKEERLEELKKKlkelEKRLEELEERHELYEEAKAKKEElerlkkrlTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 829 LEKAQLRFFEFKRRQLvKLVNLEKDLVQQKDILKKEVQEEQEILECLK-------------CEHDKEsRLLEKHDESVTD 895
Cdd:PRK03918 386 PEKLEKELEELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelTEEHRK-ELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 896 VTEvpqDFEKIKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFEI---------LDRGPLSLDNTLYQ-VEKEMEEKEE 965
Cdd:PRK03918 464 IEK---ELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLkeleeklkkYNLEELEKKAEEYEkLKEKLIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 966 QLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQ 1045
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEK 619
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2462580778 1046 KLASLNSGSREQSGLQASLEAEQEALEKDQERINAYIEEEVQRRLQDLHRVISE 1099
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
605-1158 |
3.11e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQ-RKETEIVQLQIRKQEESLKRRSFHIENKLKDL 683
Cdd:pfam12128 380 RRSKIKEQNNRDIAGIKDKLAKIREARDRQL---AVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 684 LAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam12128 457 TATPE-------------LLLQLENFDERIERAREEQEA-----ANAEVERLQ--SELRQARKRRDQASEALRQASRRLE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 764 EQEKEqvmlVAHLEEQLREKQ-EMIQLLRRGEVQWVEEEKRDLEgiRESLLR---VKEARAGGDEDGEELEKAQLRffeF 839
Cdd:pfam12128 517 ERQSA----LDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVIS--PELLHRtdlDPEVWDGSVGGELNLYGVKLD---L 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 840 KRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQS 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 920 LQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNT----LYQVEKEMEEKEEQLAQY-----QANANQLQKLQATFE-FTAN 989
Cdd:pfam12128 665 EKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAaRRSG 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 990 IARQEEKVRKKEKEILESRE---------KQQREALERALARLE-RRHSALQRH------------------STLGTEIE 1041
Cdd:pfam12128 745 AKAELKALETWYKRDLASLGvdpdviaklKREIRTLERKIERIAvRRQEVLRYFdwyqetwlqrrprlatqlSNIERAIS 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1042 EQRQKLASLNSGSREQsglQASLEAEQEALEKDQERINAYIE--EEVQRRLQDLH---------RVISEgCSTSADTMKD 1110
Cdd:pfam12128 825 ELQQQLARLIADTKLR---RAKLEMERKASEKQQVRLSENLRglRCEMSKLATLKedanseqaqGSIGE-RLAQLEDLKL 900
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 1111 NEKLHNGTIQRKLKYEITV--------LDETWTVFRRYSRFREMHKTLKLKYAELA 1158
Cdd:pfam12128 901 KRDYLSESVKKYVEHFKNViadhsgsgLAETWESLREEDHYQNDKGIRLLDYRKLV 956
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
651-843 |
3.60e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 651 QRKETEIVQlqIRKQEESLKRRsfhiENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLrVQEELQRLKELNNNE 730
Cdd:COG1579 13 QELDSELDR--LEHRLKELPAE----LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-VEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 731 KAEKfqifqELDQLQKEKDeqyaKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRE 810
Cdd:COG1579 86 RNNK-----EYEALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170 180 190
....*....|....*....|....*....|...
gi 2462580778 811 SLLRVKEARAggdEDGEELEKAQLRFFEFKRRQ 843
Cdd:COG1579 157 ELEELEAERE---ELAAKIPPELLALYERIRKR 186
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
602-1024 |
5.45e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 602 PICLRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhiENKLK 681
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK----ELLEI 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 682 DLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyAKLELEKKR 761
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE--EEEEEEKSR 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 762 LEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFfEFKR 841
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK-EEEL 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 842 RQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT-DVTEVPQDFEKIKPVEYRLQYK--ER 918
Cdd:pfam02463 836 EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSKEEKEKEEKKELEEESQKLNLleEK 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 919 QLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
410 420
....*....|....*....|....*.
gi 2462580778 999 KKEKEILESREKQQREALERALARLE 1024
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
613-870 |
6.29e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.95 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 613 QREELEKLESKRKLIEEmEEKQKSDKAELERMQQEVETQRKETEivqlqiRKQEESLKRRSFHI---ENKLKDLLAEKEK 689
Cdd:pfam15558 33 AWEELRRRDQKRQETLE-RERRLLLQQSQEQWQAEKEQRKARLG------REERRRADRREKQViekESRWREQAEDQEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 690 FEEERLREQQEIELQKKRQEEETfLRVQEE-LQRLKELNNNEKAEKFQI---------------FQELDQ---------- 743
Cdd:pfam15558 106 QRQEKLERARQEAEQRKQCQEQR-LKEKEEeLQALREQNSLQLQERLEEachkrqlkereeqkkVQENNLsellnhqark 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 744 ----LQKEKDEQYAKLELEKKRLEEQEK-EQVMLVAHLEEQLREKQEMIQLLRrgeVQWVEEEK-RDLEGIRESLLRVKE 817
Cdd:pfam15558 185 vlvdCQAKAEELLRRLSLEQSLQRSQENyEQLVEERHRELREKAQKEEEQFQR---AKWRAEEKeEERQEHKEALAELAD 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462580778 818 ARAGGDEDGEELEKAQlrffefkRRQLVKLVNLEKDLVQQkdILKKEVQEEQE 870
Cdd:pfam15558 262 RKIQQARQVAHKTVQD-------KAQRARELNLEREKNHH--ILKLKVEKEEK 305
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
613-768 |
7.61e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 613 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEE 692
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 693 ERLreqqeiELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:PRK12704 122 KQQ------ELEKKEEELEE--LIEEQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLikEIEEEAKEEADKK 189
|
|
| PX_PI3K_C2 |
cd06883 |
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ... |
1131-1202 |
8.79e-05 |
|
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.
Pssm-ID: 132793 Cd Length: 109 Bit Score: 43.11 E-value: 8.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580778 1131 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERR-SHLEKYLRDFFSVMLQSATSPL 1202
Cdd:cd06883 29 TEPSFVFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLGRSHIKQVAERRkIELNSYLKSLFNASPEVAESDL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
639-867 |
9.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 639 AELERMQQEVETQRKETEIVQlQIRKQEESLKRrsfhienkLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtflRVQE 718
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAA--------ARERLAELEYLRAALRLWFAQRRLELLEAELE---ELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 719 ELQRLKELNNNEKAEKFQIFQELDQLQkekdEQYAKLELEkkRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWV 798
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELE----AQIRGNGGD--RLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 799 EEEKrDLEGIREsllrvkEARAGGDEDGEELEKAQLRFFEFKRRqlvklvnlEKDLVQQKDILKKEVQE 867
Cdd:COG4913 377 ASAE-EFAALRA------EAAALLEALEEELEALEEALAEAEAA--------LRDLRRELRELEAEIAS 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
615-831 |
1.48e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 615 EELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEER 694
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 695 LREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyaklelekkrlEEQEKEQVMLVA 774
Cdd:TIGR02169 892 DELEAQLRELERKIEE-----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE------------DEEIPEEELSLE 954
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462580778 775 HLEEQLREKQEMIQLLrrGEV-----QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEK 831
Cdd:TIGR02169 955 DVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PX_SNX17_31 |
cd06885 |
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ... |
1139-1187 |
2.47e-04 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.
Pssm-ID: 132795 Cd Length: 104 Bit Score: 41.55 E-value: 2.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462580778 1139 RYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERvIAERRSHLEKYL 1187
Cdd:cd06885 34 RYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPLTPAQ-LEERRLQLEKYL 81
|
|
| PX_SNX27 |
cd06886 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ... |
1138-1193 |
2.54e-04 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.
Pssm-ID: 132796 Cd Length: 106 Bit Score: 41.63 E-value: 2.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 1138 RRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAeRRSHLEKYLRDFFSV 1193
Cdd:cd06886 36 RRYREFANLHQNLKKEFPDFQFPKLPGKWPFSLSEQQLDA-RRRGLEQYLEKVCSI 90
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
706-1100 |
2.57e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQEL----DQLQKEKDEQYAKLELEKKRLEEQE--KEQVMLVAH---- 775
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVidlqTKLQEMQMERDAMADIRRRESQSQEdlRNQLQNTVHelea 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 776 ----LEEQLREKQEMIQLLRRGEVQwveeEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLE 851
Cdd:pfam15921 157 akclKEDMLEDSNTQIEQLRKMMLS----HEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 852 KDLVQ--------QKDILKKEVQEEQEILecLKCEHDKESRLLEKHDESVTDVTE----VPQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam15921 233 ISYLKgrifpvedQLEALKSESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEkassARSQANSIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 920 LQYLLQNHLPTL----------LEEKQRAFE----------ILDRGPLS---------------LDNTLYQVEKEMEEKE 964
Cdd:pfam15921 311 QNSMYMRQLSDLestvsqlrseLREAKRMYEdkieelekqlVLANSELTearterdqfsqesgnLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 965 EQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQRE----ALERALARLERRHSALQRHSTLGTEI 1040
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQL 470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462580778 1041 EEQRQKL-----------ASLNSGSREQSGLQASLEAEQEALEKDQERINAyIEEEVQRRLQDLHRVISEG 1100
Cdd:pfam15921 471 ESTKEMLrkvveeltakkMTLESSERTVSDLTASLQEKERAIEATNAEITK-LRSRVDLKLQELQHLKNEG 540
|
|
| PX_SNX22 |
cd06880 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ... |
1125-1187 |
2.74e-04 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.
Pssm-ID: 132790 Cd Length: 110 Bit Score: 41.49 E-value: 2.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462580778 1125 YEITVLDE--TWTVFRRYSRFREMHKTLKLKYaelAALEFPPKKLfGNKDERVIAERRSHLEKYL 1187
Cdd:cd06880 22 FTIEVLVNgrRHTVEKRYSEFHALHKKLKKSI---KTPDFPPKRV-RNWNPKVLEQRRQGLEAYL 82
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
473-551 |
2.83e-04 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 41.04 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 473 LKEGQTYVGRDDASteqDIVLHGLDLESEHC-IFENIGGTVTLIPLSGS-QCSVNGVQIVEATHLNQGAVILLGrTNMFR 550
Cdd:cd22673 18 LTKKSCTFGRDLSC---DIRIQLPGVSREHCrIEVDENGKAYLENLSTTnPTLVNGKAIEKSAELKDGDVITIG-GRSFR 93
|
.
gi 2462580778 551 F 551
Cdd:cd22673 94 F 94
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
478-543 |
2.85e-04 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 40.25 E-value: 2.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498 1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66
|
|
| PX_SNX14 |
cd06877 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ... |
1118-1189 |
2.89e-04 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.
Pssm-ID: 132787 Cd Length: 119 Bit Score: 41.98 E-value: 2.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 1118 TIQRKLKYEITVLDETWTVFRRYSRFRemhkTLKLKYAE----LAALEFPPKKLFGNKDERVIAERRSHLEKYLRD 1189
Cdd:cd06877 28 EVERNDRRAKGHEPQHWSVLRRYNEFY----VLESKLTEfhgeFPDAPLPSRRIFGPKSYEFLESKREIFEEFLQK 99
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
607-873 |
3.16e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhIENKLKDLLAE 686
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER---ILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 687 KEKFEeerlreqqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELdqLQKEKDEQYAKLELEKKrlEEQE 766
Cdd:pfam13868 168 EEERE------------AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL--YQEEQERKERQKEREEA--EKKA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 767 KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVK 846
Cdd:pfam13868 232 RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAA 308
|
250 260
....*....|....*....|....*..
gi 2462580778 847 LVNLEkdlVQQKDILKKEVQEEQEILE 873
Cdd:pfam13868 309 EREEE---LEEGERLREEEAERRERIE 332
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
720-1099 |
3.23e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 720 LQRLKELNNNEKAEKFQIFQElDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvAHLEEQ--LREKQEMIQLLRRGEVQW 797
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVE-RRRKLEEAEKARQ---AEMDRQaaIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 798 V--EEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEEqeilecl 875
Cdd:pfam17380 353 IrqEERKRELERIRQEEIAMEISRM------RELERLQM-----ERQQKNERVRQELEAARKVKILEEERQRK------- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 876 kcehdkesrllekhdesvtdVTEVPQDFEKIKpveyRLQYKERQLQyllqnhLPTLLEEKQRAFEILDRgplsldntlyq 955
Cdd:pfam17380 415 --------------------IQQQKVEMEQIR----AEQEEARQRE------VRRLEEERAREMERVRL----------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 956 vekemeekeeqlaQYQANANQLQKLqatfeftaniaRQEEKVRKKEKEILESREKQQREALEralarlerrhsalQRHST 1035
Cdd:pfam17380 454 -------------EEQERQQQVERL-----------RQQEEERKRKKLELEKEKRDRKRAEE-------------QRRKI 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1036 LGTEIEEQRQKLAslnSGSREQSGLQASLEAEQEALEKDQERINA------YIEEEVQRRLQDLHRVISE 1099
Cdd:pfam17380 497 LEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYEEERRREAeeerrkQQEMEERRRIQEQMRKATE 563
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
608-902 |
4.41e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLIEEMEEK----------QKSDKAELERMQQEVETQRKET-EIVQLQIRKQEESLKRRSFHI 676
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKimkldneikaLKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 677 ENKLKDLLAEKEKFEEERLreqqeiELQKKRQE---EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKD---E 750
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERR------LLNQEKTEllvEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFserQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 751 QYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR---RGEVQWVEEEKRDLEGIRESLLRVKearaggdEDGE 827
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekKGLGRTIELKKEILEKKQEELKFVI-------KELQ 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 828 ELEKAQLRFFEFK---RRQLVKLVNLEKD-LVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 902
Cdd:TIGR00606 465 QLEGSSDRILELDqelRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKD 543
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
611-867 |
4.88e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELekleskRKLIEEMEEKQKSDKAELERMQ-QEVETQRKETEIVQ-----LQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG5022 806 LGSRKEY------RSYLACIIKLQKTIKREKKLREtEEVEFSLKAEVLIQkfgrsLKAKKRFSLLKKETIYLQSAQRVEL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 685 AEKEKF-------------EEERLREQQEIELQKKRQE---EETFLRVqEELQRLKELNNNEKAEkfqifqELDQLQKEK 748
Cdd:COG5022 880 AERQLQelkidvksisslkLVNLELESEIIELKKSLSSdliENLEFKT-ELIARLKKLLNNIDLE------EGPSIEYVK 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 749 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDedgeE 828
Cdd:COG5022 953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN-FKKELAELSKQYGALQESTKQLKELPVEVA----E 1027
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462580778 829 LEKAQLRFFE--FKRRQLVKLVNLEKDLVQQKDILKKEVQE 867
Cdd:COG5022 1028 LQSASKIISSesTELSILKPLQKLKGLLLLENNQLQARYKA 1068
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
611-803 |
5.54e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ-EVETQRKETEIVQlQIRKQEESLKRR--SFHIENKLKDLLAEk 687
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLRKEI----ERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 688 ekfeeerlreqqeieLQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1340 169 ---------------LKELRKEAEEI---HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462580778 768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
676-820 |
6.71e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 676 IENKLKDLLAEKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQ--LQKEK--DEQ 751
Cdd:PRK12704 36 AEEEAKRILEEAKK------------EAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQKEEnlDRK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 752 YAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLrrgevqwVEEEKRDLEGIreSLLRVKEARA 820
Cdd:PRK12704 102 LELLEKREEELEKKEKE----LEQKQQELEKKEEELEEL-------IEEQLQELERI--SGLTAEEAKE 157
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
834-1091 |
7.01e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKkEVqEEQeiLECLKCEHDKESRLLEKHDE--------SVTDVTEVPQDFEK 905
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEDILN-EL-ERQ--LKSLERQAEKAERYKELKAElrelelalLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 906 IKPVEYRLQYKERQLQYLLQNhLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFE 985
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 986 FTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQsglQASLE 1065
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ---IASLN 399
|
250 260
....*....|....*....|....*.
gi 2462580778 1066 AEQEALEKDQERINAYIEEEVQRRLQ 1091
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEE 425
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
614-924 |
7.08e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 614 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKrrsfHIENK---LKDLLAEKEKF 690
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ----HLKNEgdhLRNVQTECEAL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 691 EEERLREQQEIELQKKRQEEETFLRVQ----------EELQRLKELNNNEkaekfqifQELDQLQKEKDEQYAKLELEKK 760
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMTQLVGQhgrtagamqvEKAQLEKEINDRR--------LELQEFKILKDKKDAKIRELEA 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 761 RLEEQEKEQVMLVAHLEEQLRE----KQEMIQLLR-----RGEVQWVEEE----KRDLEGIRESL--------LRVKEAR 819
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNELNSLSEDyevlKRNFRNKSEEMetttnklkMQLKSAQ 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 820 AggdedgeELEKAQ--LRFFEFKRRQLVKL-VNLEKDLVQQK---DILKKEVQ-EEQEILECLKCEH---DKESRLLEKH 889
Cdd:pfam15921 706 S-------ELEQTRntLKSMEGSDGHAMKVaMGMQKQITAKRgqiDALQSKIQfLEEAMTNANKEKHflkEEKNKLSQEL 778
|
330 340 350
....*....|....*....|....*....|....*
gi 2462580778 890 DESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 924
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
969-1161 |
7.82e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 969 QYQANANQLQKLQATfeftanIARQEEKVRKKEKEILESREKQQREALERALARLERrhsalqrhstLGTEIEEQRQKLA 1048
Cdd:COG4913 263 RYAAARERLAELEYL------RAALRLWFAQRRLELLEAELEELRAELARLEAELER----------LEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1049 SLnSGSREQSGLQ--ASLEAEQEALEKDQERInayieEEVQRRLQDLHRVISEGCSTSADTMKDNEKLHNGTIQRKLKYE 1126
Cdd:COG4913 327 EL-EAQIRGNGGDrlEQLEREIERLERELEER-----ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|....*
gi 2462580778 1127 ITVLDETWTVFRRYSRFREMHKTLKlkyAELAALE 1161
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELE---AEIASLE 432
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
703-908 |
8.04e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIF-QELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlvahLEEQLR 781
Cdd:pfam05262 183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLkEELDKKQIDADKAQQKADFAQDNADKQRDE-------VRQKQQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 782 EKQemiQLLRRGEVQWVEEEKRDLEgiresllrvkearaggdEDGEELEKAQLrffEFKRrqlvKLVNLEKDLVQQKDIL 861
Cdd:pfam05262 256 EAK---NLPKPADTSSPKEDKQVAE-----------------NQKREIEKAQI---EIKK----NDEEALKAKDHKAFDL 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462580778 862 KKEVQEEQEILEclkcehdkesrllEKHDESVTDVTEVPQDFEKIKP 908
Cdd:pfam05262 309 KQESKASEKEAE-------------DKELEAQKKREPVAEDLQKTKP 342
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
722-1093 |
8.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 722 RLKELNNNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQL------LRRGEV 795
Cdd:COG4717 64 RKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqeLEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 796 QWVEEEKRdLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECL 875
Cdd:COG4717 140 ELAELPER-LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 876 KCEHDKesrlLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQ 955
Cdd:COG4717 219 QEELEE----LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 956 VEKEMEEKEEQLAQYQANANQLQKLQ-------------ATFEFTANIARQEEKVRKKEKEILESREKQQREALERALAR 1022
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEEleellaalglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1023 L------------ERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQS------GLQASLEAEQEALEKDQERINAYIEE 1084
Cdd:COG4717 375 LlaeagvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeeELEEELEELEEELEELEEELEELREE 454
|
410
....*....|.
gi 2462580778 1085 --EVQRRLQDL 1093
Cdd:COG4717 455 laELEAELEQL 465
|
|
| PX_RPK118_like |
cd07287 |
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ... |
1135-1191 |
8.36e-04 |
|
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.
Pssm-ID: 132820 Cd Length: 118 Bit Score: 40.33 E-value: 8.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580778 1135 TVFRRYSRFREMHKTLKLKYAELAALE--FPP---KKLFGNKDERVIAERRSHLE---------------KYLRDFF 1191
Cdd:cd07287 39 VVWKRYSDFKKLHKDLWQIHKNLCRQSelFPPfakAKVFGRFDESVIEERRQCAEdllqfsanipalynsSQLEDFF 115
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
551-820 |
8.99e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 551 FNHPKEAAKLREKRKSgllssfslsMTDLSKSRENLSAVMLYNPGLFPIKGPICLR--LEFERQQREELEKLESKrklIE 628
Cdd:PRK05771 36 LKEELSNERLRKLRSL---------LTKLSEALDKLRSYLPKLNPLREEKKKVSVKslEELIKDVEEELEKIEKE---IK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 629 EMEEKqksdKAELERMQQEVETQRKETEI-----VQLQIRKQEESLKRRSFHI-ENKLKDLLAEKEKFEEERLREQQE-- 700
Cdd:PRK05771 104 ELEEE----ISELENEIKELEQEIERLEPwgnfdLDLSLLLGFKYVSVFVGTVpEDKLEELKLESDVENVEYISTDKGyv 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 701 --IELQKKRQEEEtflrVQEELQRLkELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE 778
Cdd:PRK05771 180 yvVVVVLKELSDE----VEEELKKL-GFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462580778 779 QL---REKQEM-IQLLRRGEV----QWVEEEkrDLEGIRESLLRVKEARA 820
Cdd:PRK05771 255 YLeieLERAEAlSKFLKTDKTfaieGWVPED--RVKKLKELIDKATGGSA 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
605-764 |
9.26e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLL 684
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 685 AEKEKFEEERLREQQEIELQKKRQEE------------ETFLRVQEELQRLKELNNneKAEkfQIFQELDQLQKEKDEQY 752
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRALEPVNM--LAI--QEYEEVLKRLDELKEKR 995
|
170
....*....|..
gi 2462580778 753 AKLELEKKRLEE 764
Cdd:TIGR02169 996 AKLEEERKAILE 1007
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
452-554 |
1.08e-03 |
|
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438785 Cd Length: 113 Bit Score: 40.17 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-------VTLIPLSGSQCSV 524
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 2462580778 525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
614-864 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 614 REELEKLESKRKLIEEMEEKQKsdkaELERMQQEVETQRKETEIVQLQIRKQE-ESLKRRSFHIENKLKDLLAEKEkfee 692
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAE----RYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELE---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 693 erlreqqeiELQKKRQEeetflrVQEELQRLKE-LNNNEkaekfqiFQELDQLQKEKDEqyakLELEKKRLEEQEKEQVM 771
Cdd:COG4913 313 ---------RLEARLDA------LREELDELEAqIRGNG-------GDRLEQLEREIER----LERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 772 LVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRffEFKRRQlvklVNLE 851
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIA--SLERRK----SNIP 439
|
250
....*....|...
gi 2462580778 852 KDLVQQKDILKKE 864
Cdd:COG4913 440 ARLLALRDALAEA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
608-713 |
1.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
90 100
....*....|....*....|....*.
gi 2462580778 688 EKFEEERLREQQEIELQKKRQEEETF 713
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGF 248
|
|
| PX_SNX15 |
cd07288 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ... |
1136-1188 |
1.30e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.
Pssm-ID: 132821 Cd Length: 118 Bit Score: 39.95 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 1136 VFRRYSRFREMHKTLKLKYAEL--AALEFPP---KKLFGNKDERVIAERRSHLEKYLR 1188
Cdd:cd07288 40 VWKRYSDLKKLHGELAYTHRNLfrRQEEFPPfprAQVFGRFEAAVIEERRNAAEAMLL 97
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
598-832 |
1.31e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 598 PIKG-PICLRLEFERQQREELE-KLESKRKLIEEMEEK--QKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRS 673
Cdd:PRK02224 460 PVEGsPHVETIEEDRERVEELEaELEDLEEEVEEVEERleRAEDLVEAED---RIERLEERREDLEELIAERRETIEEKR 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 674 FHIENKLK---DLLAEKEkfeeerlreqqeielQKKRQEEETFLRVQEELQRLKELNnnekAEKFQIFQELDQLQK--EK 748
Cdd:PRK02224 537 ERAEELREraaELEAEAE---------------EKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERirTL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 749 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrRGEVQ--WVEEEKRDLEGIRESLLRVKEARAGGDEDG 826
Cdd:PRK02224 598 LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKREL-EAEFDeaRIEEAREDKERAEEYLEQVEEKLDELREER 676
|
....*.
gi 2462580778 827 EELEKA 832
Cdd:PRK02224 677 DDLQAE 682
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
608-763 |
1.38e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEvetQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:pfam17380 447 EMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRD---RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM 522
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 688 EKFEEERLREQQEIELQKKR---QEEETFLRVQEELQRLKElnnnEKAekfqifqELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERrkqQEMEERRRIQEQMRKATE----ERS-------RLEAMEREREMMRQIVESEKARAE 590
|
|
| PX_SNX16 |
cd07276 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ... |
1125-1182 |
1.52e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.
Pssm-ID: 132809 Cd Length: 110 Bit Score: 39.31 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462580778 1125 YEITVL---DETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNKDERVIAERRSH 1182
Cdd:cd07276 23 YKIRVEnkvGDSWFVFRRYTDFVRLNDKLKQMFPGF-RLSLPPKRWFKDNFDPDFLEERQL 82
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
608-829 |
1.68e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKL-------IEEMEEKQKsdKAELERMQQEVETQRKETEIVQLQ-----IRKQEESLKRRSFH 675
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLknkheamISDLEERLK--KEEKGRQELEKAKRKLEGESTDLQeqiaeLQAQIAELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 676 IENKLKDLLAEKEKFEEERLREqqeieLQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE----KDEQ 751
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNA-----LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtLDTT 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 752 YAKLELEKKRleeqEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEEL 829
Cdd:pfam01576 316 AAQQELRSKR----EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL 389
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
605-938 |
1.99e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQEVETQ-------RKETEIVQLQIR---KQEESLKRRSF 674
Cdd:pfam10174 350 LRLRLEEKES----FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKerkinvlQKKIENLQEQLRdkdKQLAGLKERVK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 675 HIEN----------KLKDLLAEKEKFEEERLREqQEIELQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQL 744
Cdd:pfam10174 426 SLQTdssntdtaltTLEEALSEKERIIERLKEQ-REREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 745 QK----------EKDEQYAKLE--LEKKRLEEQEKEQVMLVAH-LEEQLREKQEM---IQLLRRgEVQWVEEEKR----D 804
Cdd:pfam10174 502 KEhasslassglKKDSKLKSLEiaVEQKKEECSKLENQLKKAHnAEEAVRTNPEIndrIRLLEQ-EVARYKEESGkaqaE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 805 LEGIRESLLRVKEARAGGDEDGEELEKAQLRFFefkRRQLVKLVNLEkdLVQQKDiLKKEVQEEQEILECLKCEHDKESR 884
Cdd:pfam10174 581 VERLLGILREVENEKNDKDKKIAELESLTLRQM---KEQNKKVANIK--HGQQEM-KKKGAQLLEEARRREDNLADNSQQ 654
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462580778 885 LleKHDESVTDVTEVPQDFEKIK----PVEYRLQYKERQLQYLLQN---HLPTLLEEKQRA 938
Cdd:pfam10174 655 L--QLEELMGALEKTRQELDATKarlsSTQQSLAEKDGHLTNLRAErrkQLEEILEMKQEA 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
753-1084 |
2.18e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 753 AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 832
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 833 QLRFFEFK---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpv 909
Cdd:TIGR02168 756 LTELEAEIeelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER---- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 910 eyRLQYKERQLQYLLQNhlptlLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTAN 989
Cdd:TIGR02168 832 --RIAATERRLEDLEEQ-----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 990 IARQEEKVrkKEKEILESREKQqrEALERALARLERRhsalqrhstlgteIEEQRQKLASLNSGS-REQSGLQASLEAEQ 1068
Cdd:TIGR02168 905 ELESKRSE--LRRELEELREKL--AQLELRLEGLEVR-------------IDNLQERLSEEYSLTlEEAEALENKIEDDE 967
|
330
....*....|....*.
gi 2462580778 1069 EALEKDQERINAYIEE 1084
Cdd:TIGR02168 968 EEARRRLKRLENKIKE 983
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
608-873 |
2.32e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRK----ETEIVQLQIRKQEESLKRRsfhienkLKDL 683
Cdd:pfam02029 10 ERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQggldEEEAFLDRTAKREERRQKR-------LQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 684 LAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 764 EQEKEQVMLVAHLEEQLRE---------KQEMIQLLRRGEV------QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEE 828
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDekikkekkvKYESKVFLDQKRGhpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462580778 829 LEKAQLRfFEFKRRQLVKLVNLEKDLVQQK--------DILKKEVQEEQEILE 873
Cdd:pfam02029 243 FLEAEQK-LEELRRRRQEKESEEFEKLRQKqqeaelelEELKKKREERRKLLE 294
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
909-1091 |
2.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 909 VEYRLQYKERQLQY---LLQNHLPTL---LEEKQRAFEILDR--GPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:COG3206 162 LEQNLELRREEARKaleFLEEQLPELrkeLEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 981 QATFEftANIARQEEKVRKKEKEILESREKQQREALERALARLERR----HSALQRhstLGTEIEEQRQKLAS-----LN 1051
Cdd:COG3206 242 LAALR--AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnHPDVIA---LRAQIAALRAQLQQeaqriLA 316
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462580778 1052 SGSREQSGLQASLEAEQEALEKDQERINAYIEEEVQ-RRLQ 1091
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAElRRLE 357
|
|
| PX_HS1BP3 |
cd06868 |
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ... |
1135-1201 |
2.34e-03 |
|
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.
Pssm-ID: 132778 Cd Length: 120 Bit Score: 39.32 E-value: 2.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580778 1135 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFgnKDERVIAERRSHLEKYLRdFFSVMLQSATSP 1201
Cdd:cd06868 48 MVSKKYSEFEELYKKLSEKYPGTILPPLPRKALF--VSESDIRERRAAFNDFMR-FISKDEKLANCP 111
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
611-988 |
2.47e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQ------------EVETQRKETEIVQLQIRKQEESLKRrsfhIEN 678
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQ----LNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 679 KLKDLlaEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE-LQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLEL 757
Cdd:TIGR04523 343 QISQL--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSyKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 758 EKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwvEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQlRF 836
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVK--------ELIIKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQ-KE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 837 FEFKRRQLVKLVNLEKDLVQQKDILKKEV---QEEQEILECLKCEhdKESRLLEKHDESVTDVTEVpqDFEKIKPVeyrL 913
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKIsslKEKIEKLESEKKE--KESKISDLEDELNKDDFEL--KKENLEKE---I 563
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462580778 914 QYKERQLQYLLQNHlpTLLEEKQRAFEILdrgplsldntlyqvekemeekeeqLAQYQANANQLQKLQATFEFTA 988
Cdd:TIGR04523 564 DEKNKEIEELKQTQ--KSLKKKQEEKQEL------------------------IDQKEKEKKDLIKEIEEKEKKI 612
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
606-895 |
2.51e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 606 RLEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE------------ 666
Cdd:pfam07888 68 REQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvle 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 667 -----ESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEI-----ELQKKR----QEEETFLRVQEELQRLKELNNN--- 729
Cdd:pfam07888 148 retelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslskEFQELRnslaQRDTQVLQLQDTITTLTQKLTTahr 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 730 EKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE-QLREKQEMIQL------LRRGEVQW----- 797
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQaRLQAAQLTLQLadaslaLREGRARWaqere 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 798 -----VEEEKRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKeVQEEQEIL 872
Cdd:pfam07888 308 tlqqsAEADKDRIEKLSAELQRLEERL---QEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV-AQKEKEQL 383
|
330 340
....*....|....*....|...
gi 2462580778 873 ECLKCEHDKESRLLEKHDESVTD 895
Cdd:pfam07888 384 QAEKQELLEYIRQLEQRLETVAD 406
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
602-867 |
2.74e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 602 PICLR-LEFERQQREELEKLESKRKLieeMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKL 680
Cdd:TIGR00606 681 PVCQRvFQTEAELQEFISDLQSKLRL---APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 681 KDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQrlKELNNNEKAEKFQI-----------FQELDQLQKEKD 749
Cdd:TIGR00606 758 RDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQ--MELKDVERKIAQQAaklqgsdldrtVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 750 EQY----AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvQWVEEEKRDLEGIRESLLRVKEARAGGDED 825
Cdd:TIGR00606 836 HELdtvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-QFEEQLVELSTEVQSLIREIKDAKEQDSPL 914
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462580778 826 GEELEKAQLRffefkRRQLVKLVNLEKDLVQQK-DILKKEVQE 867
Cdd:TIGR00606 915 ETFLEKDQQE-----KEELISSKETSNKKAQDKvNDIKEKVKN 952
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
611-689 |
2.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
624-788 |
2.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 624 RKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQlqirkQEESLKRRSfHIENKLKDLLAEkekfeeerlreQQEIEl 703
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEA-----KEEIHKLRN-EFEKELRERRNE-----------LQKLE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEE-----QEKEQVMLVAHLEE 778
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERisgltAEEAKEILLEKVEE 165
|
170
....*....|.
gi 2462580778 779 QLR-EKQEMIQ 788
Cdd:PRK12704 166 EARhEAAVLIK 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
704-888 |
2.96e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE---QYAKLELEKKRLEEQEKEQVMLVAHLEEQL 780
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 781 REKQEMI--------------------------QLLRRGEV--QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkA 832
Cdd:COG4942 100 EAQKEELaellralyrlgrqpplalllspedflDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELE-A 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 833 QLRFFEFKRRQLVKLVNLEKDLVQQkdiLKKEVQEEQEILECLKCEHDKESRLLEK 888
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIAR 231
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
607-869 |
3.98e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 607 LEFERQQREELEKleSKRKLIEEMEEKQKSDKAELERMQQevetqRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 686
Cdd:pfam05557 43 LDRESDRNQELQK--RIRLLEKREAEAEEALREQAELNRL-----KKKYLEALNKKLNEKESQLADAREVISCLKNELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 687 kekfeeerlreqqeieLQKKRQEEETFLRVQE-ELQRLKELNNNEKA------EKFQIFQELDQLQKEKDEQYAKLELEk 759
Cdd:pfam05557 116 ----------------LRRQIQRAELELQSTNsELEELQERLDLLKAkaseaeQLRQNLEKQQSSLAEAEQRIKELEFE- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 760 krLEEQE---------KEQVMLVAHLEEQLREKQEMIQLLR--RGEVQWVEEEKrdlEGIRESLLRVKEARAGGDEDGEE 828
Cdd:pfam05557 179 --IQSQEqdseivknsKSELARIPELEKELERLREHNKHLNenIENKLLLKEEV---EDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580778 829 LEKAQLRFFEFK----------------RRQLVKLVNLEKDLVQQKDILKKEVQEEQ 869
Cdd:pfam05557 254 KEKLEQELQSWVklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLE 310
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
608-786 |
3.98e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 608 EFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhiENKLKDLLAEK 687
Cdd:pfam02029 147 TEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---GEEEVTKLKVT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 688 EKFEEERLREQQEIELQKKRQEEeTFLRVQEELQRLKELNNNE----KAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEfeklRQKQQEAELELEELKKKREERRKLLEEEEQRRK 301
|
170 180
....*....|....*....|...
gi 2462580778 764 EQEKEQvmLVAHLEEQLREKQEM 786
Cdd:pfam02029 302 QEEAER--KLREEEEKRRMKEEI 322
|
|
| PX_SNX1_2_like |
cd06859 |
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ... |
1135-1188 |
4.19e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.
Pssm-ID: 132769 [Multi-domain] Cd Length: 114 Bit Score: 38.33 E-value: 4.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 1135 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERV--IAERRSHLEKYLR 1188
Cdd:cd06859 38 SVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGRFKVKFefIEKRRAALERFLR 93
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
612-1091 |
4.57e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 612 QQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQEEslkrrsfhienklkdLLAEKEKFe 691
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLC---EEKNALQEQLQAETE---------------LCAEAEEM- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 692 eerlreqqEIELQKKRQEEETFL-----RVQEELQRLKELnNNEKAEKFQIFQELDQ-----------LQKEK------- 748
Cdd:pfam01576 63 --------RARLAARKQELEEILhelesRLEEEEERSQQL-QNEKKKMQQHIQDLEEqldeeeaarqkLQLEKvtteaki 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 749 ----------DEQYAKLELEKKRLEEQEKEQVMLVAHLEE------QLREKQEMI-----QLLRRGEVQWVEEEK--RDL 805
Cdd:pfam01576 134 kkleedilllEDQNSKLSKERKLLEERISEFTSNLAEEEEkakslsKLKNKHEAMisdleERLKKEEKGRQELEKakRKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 806 EG--------IRESLLRVKEARAGGDEDGEELEKAQLRFFE--FKRRQLVK--------LVNLEKDLVQQKDILKKEVQE 867
Cdd:pfam01576 214 EGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEetAQKNNALKkireleaqISELQEDLESERAARNKAEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 868 EQ---EILECLKCE----HDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFE 940
Cdd:pfam01576 294 RRdlgEELEALKTEledtLDTTAAQQELRSKREQEVTELK------KALEEETRSHEAQLQEMRQKH-TQALEELTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 941 ILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAN-----------QLQKLQATFEFTANIARQEEKVRKKEKEILESRE 1009
Cdd:pfam01576 367 QAKRNKANLEKAKQALESENAELQAELRTLQQAKQdsehkrkklegQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1010 KQQREAlERALARLERRHSAL--QRHSTLGTEIEEQRQKLA---SLNSGSREQSGLQASLEAEQEA-------------- 1070
Cdd:pfam01576 447 SLLNEA-EGKNIKLSKDVSSLesQLQDTQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEAkrnverqlstlqaq 525
|
570 580
....*....|....*....|....*.
gi 2462580778 1071 ---LEKDQERINAYIE--EEVQRRLQ 1091
Cdd:pfam01576 526 lsdMKKKLEEDAGTLEalEEGKKRLQ 551
|
|
| PX_p40phox |
cd06882 |
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ... |
1132-1192 |
4.61e-03 |
|
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.
Pssm-ID: 132792 Cd Length: 123 Bit Score: 38.57 E-value: 4.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1132 ETWTVFRRYSRFREMHKTLKLKY---AELAAL-----EFPPKKLFGNKDErvIAERR-SHLEKYLRDFFS 1192
Cdd:cd06882 33 SKYLIYRRYRQFFALQSKLEERFgpeAGSSAYdctlpTLPGKIYVGRKAE--IAERRiPLLNRYMKELLS 100
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
605-764 |
4.70e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.87 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 605 LRLEFERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETQRKETEivqlqiRKQEESLKRRsfhienklkdlL 684
Cdd:pfam05672 23 AREQREREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE------RRREEEERQR-----------K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 685 AEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLkelnnnekaEKFQIFQELDQLQKEKdeqyakleleKKRLEE 764
Cdd:pfam05672 81 AEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER----------KKRIEE 141
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
618-861 |
4.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 618 EKLESKRKLIEEMEEKQKSDKAELERMqqeVETQRKETEivqlQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLRE 697
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNK---YDELVEEAK----TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 698 QQEIELQKKrqeEETFLRVQEE----LQRLKElnNNEKAEKfqIFQELDQLQKekdeqyaKLELEKKRLEEQEKeqvmlv 773
Cdd:PHA02562 268 KSKIEQFQK---VIKMYEKGGVcptcTQQISE--GPDRITK--IKDKLKELQH-------SLEKLDTAIDELEE------ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 774 ahLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVK----EARAGGDEDGEELEKAQlrffefkrRQLVKLVN 849
Cdd:PHA02562 328 --IMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKaaieELQAEFVDNAEELAKLQ--------DELDKIVK 393
|
250
....*....|..
gi 2462580778 850 LEKDLVQQKDIL 861
Cdd:PHA02562 394 TKSELVKEKYHR 405
|
|
| PX_SNX21 |
cd07301 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a ... |
1138-1193 |
5.04e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.
Pssm-ID: 132834 Cd Length: 112 Bit Score: 38.25 E-value: 5.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580778 1138 RRYSRFREMHKTLKLKY-AELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSV 1193
Cdd:cd07301 40 RRYSDFERLHRRLRRLFgGEMAGVSFPRKRLRKNFTAETIAKRSRAFEQFLCHLHSL 96
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
621-772 |
5.28e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 621 ESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEiVQLQIRKQEESLKRRSFHIENklkdllAEKEKFEEERLREQQE 700
Cdd:pfam02029 206 EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE-VFLEAEQKLEELRRRRQEKES------EEFEKLRQKQQEAELE 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462580778 701 IELQKKRQEEETFLRVQEELQRlkelnNNEKAEKfqifqeldQLQKEKDEQYAKLELEKKRLEEQEKEQVML 772
Cdd:pfam02029 279 LEELKKKREERRKLLEEEEQRR-----KQEEAER--------KLREEEEKRRMKEEIERRRAEAAEKRQKLP 337
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
615-768 |
5.34e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 615 EELEKL-ESKRKLIEEMEEKQKSDKAELERMQQEVEtqRKETEIVQLQIRKQE-------------------ESLKRRSF 674
Cdd:TIGR04523 457 KNLDNTrESLETQLKVLSRSINKIKQNLEQKQKELK--SKEKELKKLNEEKKEleekvkdltkkisslkekiEKLESEKK 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 675 HIENKLKDLLAEKEKFEEERLREQQEIELQKKrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK 754
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDEK----------NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
170
....*....|....
gi 2462580778 755 LELEKKRLEEQEKE 768
Cdd:TIGR04523 605 IEEKEKKISSLEKE 618
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
931-1093 |
6.34e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 931 LLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaNIARQEEKVRkkekeilesREK 1010
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE---ELEAELEELR---------EEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1011 QQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERINAYIEEEVQRRL 1090
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
...
gi 2462580778 1091 QDL 1093
Cdd:COG4717 199 EEL 201
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
618-818 |
6.99e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 618 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 697
Cdd:cd16269 87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 698 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHL 776
Cdd:cd16269 155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462580778 777 EEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:cd16269 229 EDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
604-1185 |
7.54e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 604 CLRLEFERQQREELEKLESKRKLIEEMEEKqksDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRS----FHIENK 679
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQL---NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgyFPNKKQ 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 680 LKDLLAEKEKfeeerlreqqeielqKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE------KDEQYA 753
Cdd:TIGR00606 575 LEDWLHSKSK---------------EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEES 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 754 KLELEKKRLEEQEKEQVMLVA-------HLEEQLREKQEMIQLLRRgeVQWVEEEKRDLEGIRESLLRVKEARAggdedg 826
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGatavysqFITQLTDENQSCCPVCQR--VFQTEAELQEFISDLQSKLRLAPDKL------ 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 827 EELEKaQLRFFEFKRRQLVKLVNLEKDLVQQKDilkKEVQEEQEILECLKCEHDKESRLLEKHDESV------------- 893
Cdd:TIGR00606 712 KSTES-ELKKKEKRRDEMLGLAPGRQSIIDLKE---KEIPELRNKLQKVNRDIQRLKNDIEEQETLLgtimpeeesakvc 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 894 -TDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlptlleekqrafeildrgPLSLDNTLYQVEKEMEEKEEQLAQYQA 972
Cdd:TIGR00606 788 lTDVTIMERFQMELKDVERKIAQQAAKLQ------------------------GSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 973 NANQLQKLQATfeftaniARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGTEIEEQRQKLASLNS 1052
Cdd:TIGR00606 844 KIELNRKLIQD-------QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 1053 GSRE-QSGLQASLEAEQEALEKDQERINAyIEEEVQRR---LQDLHRVISEGCStsaDTMKDNEKLHNGTI--------- 1119
Cdd:TIGR00606 917 FLEKdQQEKEELISSKETSNKKAQDKVND-IKEKVKNIhgyMKDIENKIQDGKD---DYLKQKETELNTVNaqleecekh 992
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580778 1120 QRKLKYEITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEK 1185
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK 1058
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
623-768 |
7.72e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 623 KRKLIEEMEEKQKSdKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKlKDLLAEKEKfeeerlrEQQEIE 702
Cdd:pfam12072 52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKK-EESLEKKEK-------ELEAQQ 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580778 703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:pfam12072 120 QQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL--LDEVEEELRHEAAVMikEIEEEAKEEADKK 185
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
611-727 |
8.88e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.13 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580778 611 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQ-EVETQRKETE-IVQLQIRKQEESlkrrsfhIENKLKDLLAEKE 688
Cdd:pfam09731 319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFErEREEIRESYEeKLRTELERQAEA-------HEEHLKDVLVEQE 389
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462580778 689 kfeeerlreqqeIELQKKRQEEETFLRVQEELQRLKELN 727
Cdd:pfam09731 390 ------------IELQREFLQDIKEKVEEERAGRLLKLN 416
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
612-689 |
9.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 9.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580778 612 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:PRK12704 68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| |
